(data stored in ACNUC7421 zone)

SWISSPROT: A4AVG8_MARSH

ID   A4AVG8_MARSH            Unreviewed;       413 AA.
AC   A4AVG8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
DE            Short=DAP decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000256|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
GN   Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120};
GN   OrderedLocusNames=FB2170_00950 {ECO:0000313|EMBL:EAR00190.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00190.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00190.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + meso-2,6-diaminopimelate = CO2 + L-lysine;
CC         Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02120,
CC         ECO:0000256|RuleBase:RU003738};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02120,
CC         ECO:0000256|RuleBase:RU003738, ECO:0000256|SAAS:SAAS00373528};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. LysA subfamily. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02120}.
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DR   EMBL; CP002157; EAR00190.1; -; Genomic_DNA.
DR   RefSeq; WP_013304885.1; NC_014472.1.
DR   STRING; 313603.FB2170_00950; -.
DR   EnsemblBacteria; EAR00190; EAR00190; FB2170_00950.
DR   KEGG; fbc:FB2170_00950; -.
DR   eggNOG; ENOG4105CU5; Bacteria.
DR   eggNOG; COG0019; LUCA.
DR   HOGENOM; HOG000045070; -.
DR   KO; K01586; -.
DR   OMA; VVGYICE; -.
DR   OrthoDB; 861683at2; -.
DR   BioCyc; MSP313603:G1GNS-456-MONOMER; -.
DR   UniPathway; UPA00034; UER00027.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_02120; LysA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01181; DAPDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01048; lysA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AVG8.
DR   SWISS-2DPAGE; A4AVG8.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|RuleBase:RU003738};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02120,
KW   ECO:0000256|SAAS:SAAS00272807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   DOMAIN       18    354       Orn_DAP_Arg_deC. {ECO:0000259|Pfam:
FT                                PF00278}.
FT   DOMAIN       23    266       Orn_Arg_deC_N. {ECO:0000259|Pfam:
FT                                PF02784}.
FT   BINDING     218    218       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
FT   BINDING     298    298       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     302    302       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     329    329       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   BINDING     356    356       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02120}.
FT   BINDING     356    356       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02120}.
FT   MOD_RES      49     49       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02120}.
SQ   SEQUENCE   413 AA;  46210 MW;  9453F621F7C3D6D6 CRC64;
     MRNADLLKIA KTYGNPVYVY DSEKIISQFN RLTNAFKGVN QLKLNYAAKA LSNIAILRLM
     NSLGSGLDTV SIQEVQLGLL AGFKPESIIF TPNGVSLEEI EEAAKLGVQI NIDNLSVLEQ
     FGGKHPDIPV CIRINPHVMA GGNSNISVGH IDSKFGISIH QIPHLLRIVE LTKMNINGIH
     MHTGSDILDI DVFLYASEIL FETAKNFKNL DFIDFGSGFK VPYKEGDIET NIEELGKKLT
     GRFNEFCKEY GKELTLAFEP GKFLVSEAGH FLAKVNVVKQ TTSTVFASVD SGFNHLIRPM
     LYGASHTIEN ISNPQGRERY YSVVGYICET DTFGNNRRIN EISEGDILCF KNAGAYCFTM
     ASNYNSRYRP AEVLWHDDKA HLIRERETFD DLIKNQVDVK DLFVPEKVKV AVK
//

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